메뉴 건너뛰기




Volumn 77, Issue 2, 1999, Pages 829-841

Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the lipid bilayer

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; HISTIDINE; LIPID; PEPTIDE; ZINC ION;

EID: 0032796075     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76935-3     Document Type: Article
Times cited : (52)

References (58)
  • 1
    • 77956710458 scopus 로고    scopus 로고
    • Liposome fusion
    • R. M. Epand, editor. Academic Press, San Diego.
    • Bailey, A. L., and P. R. Cullis. 1998. Liposome fusion. In Current Topics in Membranes, Vol. 44. R. M. Epand, editor. Academic Press, San Diego. 359-373.
    • (1998) Current Topics in Membranes , vol.44 , pp. 359-373
    • Bailey, A.L.1    Cullis, P.R.2
  • 3
    • 77956686958 scopus 로고    scopus 로고
    • Morphology of membrane fusion
    • R. M. Epand, editor. Academic Press, San Diego.
    • Burger, K. N. J. 1998. Morphology of membrane fusion. In Current Topics in Membranes, Vol. 44. R. M. Epand, editor. Academic Press, San Diego. 403-445.
    • (1998) Current Topics in Membranes , vol.44 , pp. 403-445
    • Burger, K.N.J.1
  • 5
    • 0030790364 scopus 로고    scopus 로고
    • Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers
    • Colotto, A., and R. M. Epand. 1997. Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers. Biochemistry. 36:7644-7651.
    • (1997) Biochemistry , vol.36 , pp. 7644-7651
    • Colotto, A.1    Epand, R.M.2
  • 6
    • 0032554642 scopus 로고    scopus 로고
    • Modulation of lipid polymorphism by the feline leukemia virus fusion peptide: Implications for the fusion mechanism
    • Davies, S. M. A., R. F. Epand, J. P. Bradshaw, and R. M. Epand. 1998a. Modulation of lipid polymorphism by the feline leukemia virus fusion peptide: implications for the fusion mechanism. Biochemistry. 37: 5720-5729.
    • (1998) Biochemistry , vol.37 , pp. 5720-5729
    • Davies, S.M.A.1    Epand, R.F.2    Bradshaw, J.P.3    Epand, R.M.4
  • 7
    • 0032478582 scopus 로고    scopus 로고
    • Structural plasticity of the feline leukemia virus fusion peptide: A circular dichroism study
    • Davies, S. M. A., S. M. Kelly, N. C. Price, and J. P. Bradshaw. 1998b. Structural plasticity of the feline leukemia virus fusion peptide: a circular dichroism study. FEBS Lett. 425:415-418.
    • (1998) FEBS Lett. , vol.425 , pp. 415-418
    • Davies, S.M.A.1    Kelly, S.M.2    Price, N.C.3    Bradshaw, J.P.4
  • 8
    • 0025013025 scopus 로고
    • Specific recognition of sulfate esters by bindin, a sperm adhesion protein from sea urchins
    • DeAngelis, P. L., and C. G. Glabe. 1990a. Specific recognition of sulfate esters by bindin, a sperm adhesion protein from sea urchins. Biochim. Biophys. Acta. 1037:100-105.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 100-105
    • DeAngelis, P.L.1    Glabe, C.G.2
  • 9
    • 0025389115 scopus 로고
    • Zinc specifically stimulates the selective binding of a peptide analogue of bindin to sulfated fucans
    • DeAngelis, P. L., and C. G. Glabe. 1990b. Zinc specifically stimulates the selective binding of a peptide analogue of bindin to sulfated fucans. Pept. Res. 3:1-7.
    • (1990) Pept. Res. , vol.3 , pp. 1-7
    • DeAngelis, P.L.1    Glabe, C.G.2
  • 10
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell, S. R., I. Martin, J.-M. Ruysschaert, Y. Shai, and R. Blumenthal 1997. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. Mol. Membr. Biol. 14:97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.-M.3    Shai, Y.4    Blumenthal, R.5
  • 12
    • 0030198517 scopus 로고    scopus 로고
    • Amyloid in Alzheimer's disease and prion-related encephalopathies: Studies with synthetic peptides
    • Forloni, G., F. Tagliavini, O. Bugiani, and M. Salmona. 1996. Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides. Prog. Neurobiol. 49:287-315.
    • (1996) Prog. Neurobiol. , vol.49 , pp. 287-315
    • Forloni, G.1    Tagliavini, F.2    Bugiani, O.3    Salmona, M.4
  • 13
    • 0021919206 scopus 로고
    • Interaction of the sperm adhesive protein, bindin, with phospholipid vesicles. I
    • Glabe, C. G. 1985a. Interaction of the sperm adhesive protein, bindin, with phospholipid vesicles. I. J. Cell. Biol. 100:794-799.
    • (1985) J. Cell. Biol. , vol.100 , pp. 794-799
    • Glabe, C.G.1
  • 14
    • 0021955353 scopus 로고
    • Interaction of the sperm adhesive protein, bindin, with phospholipid vesicles. II
    • Glabe, C. G. 1985b. Interaction of the sperm adhesive protein, bindin, with phospholipid vesicles. II. J. Cell. Biol. 100:800-806.
    • (1985) J. Cell. Biol. , vol.100 , pp. 800-806
    • Glabe, C.G.1
  • 15
    • 0039256708 scopus 로고    scopus 로고
    • NMR and CD structural analysis of the fusogenic peptide sequence B18 from the fertilization protein bindin
    • Glaser, R., M. Grüne, C. Wandelt, and A. S. Ulrich. 1999. NMR and CD structural analysis of the fusogenic peptide sequence B18 from the fertilization protein bindin. Biochemistry. 38:2560-2569.
    • (1999) Biochemistry , vol.38 , pp. 2560-2569
    • Glaser, R.1    Grüne, M.2    Wandelt, C.3    Ulrich, A.S.4
  • 16
    • 0026743982 scopus 로고
    • The ammo-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation, and aggregation
    • Gordon, L. M., C. C. Curtain, Y. C. Zhong, A. Kirkpatrick, P. W. Mobley, and A. J. Waring. 1992. The ammo-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation, and aggregation. Biochim. Biophys. Acta. 1139:257-274.
    • (1992) Biochim. Biophys. Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 17
    • 0030012221 scopus 로고    scopus 로고
    • Effect of N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
    • Gray, C., S. A. Tatulian, S. A. Wharton, and L. K. Tamm. 1996. Effect of N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophys. J. 70:2275-2286.
    • (1996) Biophys. J. , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 19
    • 0000287894 scopus 로고
    • Bindin, a multifunctional sperm ligand and the evolution of new species
    • Hofmann, A., and C. G. Glabe. 1994. Bindin, a multifunctional sperm ligand and the evolution of new species. Semin. Dev. Biol. 5:233-242.
    • (1994) Semin. Dev. Biol. , vol.5 , pp. 233-242
    • Hofmann, A.1    Glabe, C.G.2
  • 20
    • 0029156388 scopus 로고
    • Molecular mechanisms of protein-mediated membrane fusion
    • Hughson, F. M. 1995. Molecular mechanisms of protein-mediated membrane fusion. Curr. Opin. Struct. Biol. 5:507-513.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 507-513
    • Hughson, F.M.1
  • 21
    • 0030966536 scopus 로고    scopus 로고
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophys. J. 73:67-75.
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 22
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly, J. W. 1997. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure. 5:595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 23
    • 0031010455 scopus 로고    scopus 로고
    • Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion
    • Kliger, Y., A. Aharoni, D. Rapaport, P. Jones, R. Blumenthal, and Y. Shai. 1997. Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion. J. Biol. Chem. 272:13496-13505.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13496-13505
    • Kliger, Y.1    Aharoni, A.2    Rapaport, D.3    Jones, P.4    Blumenthal, R.5    Shai, Y.6
  • 24
    • 0029001091 scopus 로고
    • Neuronal membrane conductance activated by amyloid β peptide: Importance of peptide conformation
    • Li, W. Y., D. L. Czilly, and L. K. Simmons. 1995. Neuronal membrane conductance activated by amyloid β peptide: importance of peptide conformation. Brain Res. 682:207-211.
    • (1995) Brain Res. , vol.682 , pp. 207-211
    • Li, W.Y.1    Czilly, D.L.2    Simmons, L.K.3
  • 25
    • 0030444084 scopus 로고    scopus 로고
    • Protein binding to supported lecithin bilayers controlled by the lipid phase state: A new concept for highly selective protein purification
    • Loidl-Stahlhofen, A., A. S. Ulrich, S. Kaufmann, and T. M. Bayert. 1996. Protein binding to supported lecithin bilayers controlled by the lipid phase state: a new concept for highly selective protein purification. Eur. Biophys. J. 25:151-153.
    • (1996) Eur. Biophys. J. , vol.25 , pp. 151-153
    • Loidl-Stahlhofen, A.1    Ulrich, A.S.2    Kaufmann, S.3    Bayert, T.M.4
  • 26
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B., H. Inouye, K. E. Szumowski, and D. Kirschner. 1998. Structural analysis of Alzheimer's β(1-40) amyloid: protofilament assembly of tubular fibrils. Biophys. J. 74:537-545.
    • (1998) Biophys. J. , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.4
  • 28
    • 0029861772 scopus 로고    scopus 로고
    • Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides
    • McLaurin, J., and A. Chakrabartty. 1996. Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. J. Biol. Chem. 271:26482-26489.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26482-26489
    • McLaurin, J.1    Chakrabartty, A.2
  • 29
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest
    • McLaurin, J., T. Franklin, A. Chakrabartty, and P. E. Fraser. 1998. Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest. J. Mol. Biol. 278:183-194.
    • (1998) J. Mol. Biol. , vol.278 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 30
    • 0032918064 scopus 로고    scopus 로고
    • Morphological transitions of brain sphingomyelin are determined by the hydration protocol: Ripples re-arrange in-plane and sponge-like networks disintegrate into small vesicles
    • Meyer, H. W., H. Bunjes, and A. S. Ulrich. 1999. Morphological transitions of brain sphingomyelin are determined by the hydration protocol: ripples re-arrange in-plane and sponge-like networks disintegrate into small vesicles. Chem. Phys. Lipids. 99:111-123.
    • (1999) Chem. Phys. Lipids , vol.99 , pp. 111-123
    • Meyer, H.W.1    Bunjes, H.2    Ulrich, A.S.3
  • 31
    • 0032432471 scopus 로고    scopus 로고
    • Minimal radius of curvature of lipid bilayers in the gel phase state corresponds to the dimension of biomembrane structures "caveolae."
    • Meyer, H. W., M. Westermann, W. Richter, M. Stumpf, W. Richter, A. S. Ulrich, and C. Hoischen. 1998. Minimal radius of curvature of lipid bilayers in the gel phase state corresponds to the dimension of biomembrane structures "caveolae." J. Struct. Biol. 124:77-87.
    • (1998) J. Struct. Biol. , vol.124 , pp. 77-87
    • Meyer, H.W.1    Westermann, M.2    Richter, W.3    Stumpf, M.4    Richter, W.5    Ulrich, A.S.6    Hoischen, C.7
  • 32
    • 0027516985 scopus 로고
    • Species-specific inhibition of fertilization by a peptide derived from the sperm protein bindin
    • Minor, J. E., R. J. Britten, and E. H. Davidson. 1993. Species-specific inhibition of fertilization by a peptide derived from the sperm protein bindin. Mol. Biol. Cell. 4:375-387.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 375-387
    • Minor, J.E.1    Britten, R.J.2    Davidson, E.H.3
  • 34
    • 0027518669 scopus 로고
    • Characterization of the membrane-associating domain of the sperm adhesive protein bindin
    • Miraglia, S. J., and C. G. Glabe. 1993. Characterization of the membrane-associating domain of the sperm adhesive protein bindin. Biochim. Biophys. Acta. 1145:191-198.
    • (1993) Biochim. Biophys. Acta , vol.1145 , pp. 191-198
    • Miraglia, S.J.1    Glabe, C.G.2
  • 35
    • 0030222281 scopus 로고    scopus 로고
    • The fusion pore and mechanisms of biological membrane fusion
    • Monck, J. R., and J. M. Fernandez. 1996. The fusion pore and mechanisms of biological membrane fusion. Curr. Opin. Cell Biol. 8:524-533.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 524-533
    • Monck, J.R.1    Fernandez, J.M.2
  • 36
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga, A., W. Neugebauer, T. Hirama, and W. K. Surewicz. 1994. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry. 33:4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 37
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Structural requirements for fusion and leakage
    • Nieva, J. L., S. Nir, A. Muga, F. M. Goni, and J. Wilschut. 1994. Interaction of the HIV-1 fusion peptide with phospholipid vesicles: structural requirements for fusion and leakage. Biochemistry. 33: 3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 38
    • 0030788927 scopus 로고    scopus 로고
    • Membrane interaction of synthetic peptides related to the putative fusogenic region of PH-30, a protein in sperm-egg fusion
    • Niidome, T., M. Kimura, T. Chiba, N. Ohmori, H. Mihara, and H. Aoyagi. 1997. Membrane interaction of synthetic peptides related to the putative fusogenic region of PH-30, a protein in sperm-egg fusion. J. Pept. Res. 49:563-569.
    • (1997) J. Pept. Res. , vol.49 , pp. 563-569
    • Niidome, T.1    Kimura, M.2    Chiba, T.3    Ohmori, N.4    Mihara, H.5    Aoyagi, H.6
  • 39
    • 0032546590 scopus 로고    scopus 로고
    • Probe transfer with and without membrane fusion in a fluorescence fusion assay
    • Ohki, S., T. D. Flanagan, and D. Hoekstra. 1998. Probe transfer with and without membrane fusion in a fluorescence fusion assay. Biochemistry. 37:7496-7503.
    • (1998) Biochemistry , vol.37 , pp. 7496-7503
    • Ohki, S.1    Flanagan, T.D.2    Hoekstra, D.3
  • 40
    • 0037926157 scopus 로고    scopus 로고
    • Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion
    • Pécheur, E. I., J. Sainte-Marie, A. Bienvenue, and D. Hoekstra. 1999. Peptides and membrane fusion: towards an understanding of the molecular mechanism of protein-induced fusion. J. Membr. Bid. 167:1-17.
    • (1999) J. Membr. Bid. , vol.167 , pp. 1-17
    • Pécheur, E.I.1    Sainte-Marie, J.2    Bienvenue, A.3    Hoekstra, D.4
  • 41
    • 0342506479 scopus 로고    scopus 로고
    • Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects
    • Pereira, F. B., F. M. Goni, A. Muga, and J. L. Nieva. 1997. Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects. Biophys. J. 73:1977-1986.
    • (1997) Biophys. J. , vol.73 , pp. 1977-1986
    • Pereira, F.B.1    Goni, F.M.2    Muga, A.3    Nieva, J.L.4
  • 43
    • 0014804933 scopus 로고
    • Membrane splitting in freeze-etching
    • Pinto-da-Silva, P., and D. Branton. 1970. Membrane splitting in freeze-etching. J. Cell Biol. 45:598-605.
    • (1970) J. Cell Biol. , vol.45 , pp. 598-605
    • Pinto-Da-Silva, P.1    Branton, D.2
  • 44
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski, M., J. D. Lear, and W. F. DeGrado. 1990. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry. 29:7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 45
    • 0025719093 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phospholipid vesicles
    • Rafalski, M., A. Rockwell, L. C. van Ginkel, J. D. Lear, W. F. DeGrado, and J. Wilschut. 1991. Membrane fusion activity of the influenza virus hemagglutinin: interaction of HA2 N-terminal peptides with phospholipid vesicles. Biochemistry. 30:10211-10220.
    • (1991) Biochemistry , vol.30 , pp. 10211-10220
    • Rafalski, M.1    Rockwell, A.2    Van Ginkel, L.C.3    Lear, J.D.4    DeGrado, W.F.5    Wilschut, J.6
  • 46
    • 0028306273 scopus 로고
    • Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes
    • Rapaport, D., and Y. Shai. 1994. Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes. J. Biol. Chem. 269:15124-15131.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15124-15131
    • Rapaport, D.1    Shai, Y.2
  • 47
    • 0029016430 scopus 로고
    • Protein design: Novel metal binding sites
    • Regan, L. 1995. Protein design: novel metal binding sites. Trends Biochem. Sci. 20:280-285.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 48
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. 1995. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20:460-464.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 50
    • 0025369546 scopus 로고
    • Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implications of α-helix formation for membrane fusion
    • Takahashi, S. 1990. Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implications of α-helix formation for membrane fusion. Biochemistry. 29:6257-6264.
    • (1990) Biochemistry , vol.29 , pp. 6257-6264
    • Takahashi, S.1
  • 51
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer ß-amyloid peptide (1-40) with lipid membranes
    • Terzi, E., G. Hölzemann, and J. Seelig. 1997. Interaction of Alzheimer ß-amyloid peptide (1-40) with lipid membranes. Biochemistry. 36: 14845-14852.
    • (1997) Biochemistry , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 52
    • 0014801016 scopus 로고
    • Demonstration of the outer surface of freeze-etched red blood cell membranes
    • Tillack, W. T., and V. T. Marchesi. 1970. Demonstration of the outer surface of freeze-etched red blood cell membranes. J. Cell Biol. 45: 649-653.
    • (1970) J. Cell Biol. , vol.45 , pp. 649-653
    • Tillack, W.T.1    Marchesi, V.T.2
  • 53
    • 0025072806 scopus 로고
    • Gramicidin a induced fusion of large unilamellar dioleoylphosphatidylcholine vesicles and its relation to the induction of type II nonbilayer structures
    • Tournois, H., C. H. J. P. Fabrie, K. N. J. Burger, J. mandersloot, P. Hilgers, H. van Delen, J. de Gier, and B. de Kruiff. 1990. Gramicidin A induced fusion of large unilamellar dioleoylphosphatidylcholine vesicles and its relation to the induction of type II nonbilayer structures. Biochemistry. 29:8297-8307.
    • (1990) Biochemistry , vol.29 , pp. 8297-8307
    • Tournois, H.1    Fabrie, C.H.J.P.2    Burger, K.N.J.3    Mandersloot, J.4    Hilgers, P.5    Van Delen, H.6    De Gier, J.7    De Kruiff, B.8
  • 54
    • 0032479148 scopus 로고    scopus 로고
    • Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin
    • Ulrich, A. S., M. Otter, C. G. Glabe, and D. Hoekstra. 1998. Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin. J. Biol. Chem. 273:16748-16755.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16748-16755
    • Ulrich, A.S.1    Otter, M.2    Glabe, C.G.3    Hoekstra, D.4
  • 58
    • 77956712809 scopus 로고    scopus 로고
    • Membrane fusion intermediates
    • R. M. Epand, editor. Academic Press, San Diego
    • Yeagle, P. L. 1998. Membrane fusion intermediates. In Current Topics in Membranes, Vol. 44. R. M. Epand, editor. Academic Press, San Diego. 375-401.
    • (1998) Current Topics in Membranes , vol.44 , pp. 375-401
    • Yeagle, P.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.